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Zinc in PDB 6r6f: Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4- Chloro-2-Cyclohexylsulfanyl-N-(2-Hydroxyethyl)-5-Sulfamoyl-BenzamideEnzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4- Chloro-2-Cyclohexylsulfanyl-N-(2-Hydroxyethyl)-5-Sulfamoyl-Benzamide
All present enzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4- Chloro-2-Cyclohexylsulfanyl-N-(2-Hydroxyethyl)-5-Sulfamoyl-Benzamide:
4.2.1.1; Protein crystallography data
The structure of Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4- Chloro-2-Cyclohexylsulfanyl-N-(2-Hydroxyethyl)-5-Sulfamoyl-Benzamide, PDB code: 6r6f
was solved by
A.Smirnov,
E.Manakova,
S.Grazulis,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6r6f:
The structure of Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4- Chloro-2-Cyclohexylsulfanyl-N-(2-Hydroxyethyl)-5-Sulfamoyl-Benzamide also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4- Chloro-2-Cyclohexylsulfanyl-N-(2-Hydroxyethyl)-5-Sulfamoyl-Benzamide
(pdb code 6r6f). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4- Chloro-2-Cyclohexylsulfanyl-N-(2-Hydroxyethyl)-5-Sulfamoyl-Benzamide, PDB code: 6r6f: Zinc binding site 1 out of 1 in 6r6fGo back to Zinc Binding Sites List in 6r6f
Zinc binding site 1 out
of 1 in the Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4- Chloro-2-Cyclohexylsulfanyl-N-(2-Hydroxyethyl)-5-Sulfamoyl-Benzamide
Mono view Stereo pair view
Reference:
D.Sribar,
M.Grabowski,
M.S.Murgueitio,
M.Bermudez,
G.Weindl,
G.Wolber.
Identification and Characterization of A Novel Chemotype For Human TLR8 Inhibitors. Eur.J.Med.Chem. V. 179 744 2019.
Page generated: Wed Dec 16 12:36:16 2020
ISSN: ISSN 0223-5234 PubMed: 31284084 DOI: 10.1016/J.EJMECH.2019.06.084 |
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